Alpha-1-Antitrypsin A1AT Paired Antibody Set
Affinity’s Alpha-1-Antitrypsin A1AT Paired Antibody Set consists of matched capture and detecting antibodies that have been titrated and optimized for use in sandwich style ELISA assays. The product as provided contains sufficient capture and detecting antibodies for five full 96-well microplates and contains a detailed protocol sheet containing directions for use, recipes for solutions and sources for additional materials required. This Alpha-1-Antitrypsin A1AT Paired Antibody Set is intended to facilitate the end user in establishing an “in-house” immunoassay for research purposes only and must not be used for diagnostic applications. Assay validation is the responsibility of the end user.
Product Code: A1AT-EIA
- Capture Antibody (A1AT-EIA-C): One yellow-capped vial containing 0.5 ml of polyclonal affinity purified anti-A1AT antibody for coating plates.
- Detecting Antibody (A1AT-EIA-D): One red-capped tube containing 0.5 ml of peroxidase conjugated affinity-purified polyclonal anti-A1AT antibody for detection of captured Alpha-1-Antitrypsin.
Related Products: VisuLize Buffer Pak
Species Cross Reactivity: View Chart
Product Datasheet: Alpha-1-Antitrypsin A1AT Matched Pair Antibody Set for ELISA
Description of Alpha 1-Antitrypsin A1AT
Alpha-1-Antitrypsin A1AT, also known as Alpha-1-Proteinase inhibitor (A1PI), is the most abundant protease inhibitor in blood and a member of the SERPIN family of proteinase inhibitors. Serum levels are typically 1.3 mg/ml (25 μM) but A1AT is an acute phase protein and concentrations can rise four-fold during inflammatory episodes or tissue injury. Low levels in circulation have been associated with pulmonary disease such as emphysema. A1AT is a single chain molecule with a mass of 52,000 daltons that is produced primarily in the liver and to a lesser extent by blood monocytes and intestinal epithelium. Based on association rates, the primary target enzyme for A1AT is believed to be neutrophil elastase1,2, but A1AT is a broad-spectrum inhibitor for many serine proteinases and the main role of A1AT in vivo is likely that of a “backup” inhibitor and proteinase scavenger in fluids and tissues. Although the association rates of A1AT with other enzymes are lower, the high concentration in plasma makes it an important inhibitor of activated Protein C, activated FXI, thrombin and plasmin1-4. Enzyme inhibition by A1AT occurs through proteolytic cleavage between Met358 and Ser359, which induces a conformational change in A1AT locking the enzyme into a stable, inactive 1:1 enzyme-inhibitor complex.
References and Reviews
- Johnson D, Travis J; Oxidative Inactivation of Human α-1-Proteinase Inhibitor; JBC 254, pp4022-4026, 1979.
- Travis J, Johnson D; Human α-1-Proteinase Inhibitor; Methods in Enzymology, 80, pp 754-765, 1981.
- Heeb MJ, Griffin JH; Physiologic Inhibition of Human Activated Protein C by α-1-Trypsin Inhibitor; JBC 263, pp11613-11616, 1988.
- Scott CF, Schapira M, James HL, Cohen AB, Colman RW; The Inactivation of Factor XIa by plasma protease inhibitors: Predominant role of α1protease inhibitor and protective effect of high molecular weight kininogen. J Clin Invest 69, pp 844, 1982.